FtsA

• Description: cell-division protein, membrane anchor for FtsZ
  
  

Gene name	ftsA
Synonyms	spoIIN
Essential	yes PubMed
Product	cell-division protein
Function	formation of Z-ring
Interactions involving this protein in SubtInteract: FtsA
MW, pI	47 kDa, 5.094
Gene length, protein length	1320 bp, 440 aa
Immediate neighbours	sbp, ftsZ
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

cell division, essential genes, membrane proteins

This gene is a member of the following regulons

SigH regulon, WalR regulon

The gene

Basic information

• Locus tag: BSU15280

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ftsA/mreB family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • FtsZ-FtsA

• Localization:
  • septal at the cell membrane PubMed
  • septal localization depends on the proton motive force PubMed

Database entries

• Structure:

• UniProt: P28264

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ftsA-ftsZ PubMed

• Sigma factor: SigA PubMed, SigH PubMed

• Regulation:
  • activated by WalR PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original Publications

Henrik Strahl, Leendert W Hamoen
Membrane potential is important for bacterial cell division.
Proc Natl Acad Sci U S A: 2010, 107(27);12281-6
[PubMed:20566861] [WorldCat.org] [DOI] (I p)

José Roberto Tavares, Robson F de Souza, Guilherme Louzada Silva Meira, Frederico J Gueiros-Filho
Cytological characterization of YpsB, a novel component of the Bacillus subtilis divisome.
J Bacteriol: 2008, 190(21);7096-107
[PubMed:18776011] [WorldCat.org] [DOI] (I p)

Shu Ishikawa, Yoshikazu Kawai, Konosuke Hiramatsu, Masayoshi Kuwano, Naotake Ogasawara
A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis.
Mol Microbiol: 2006, 60(6);1364-80
[PubMed:16796675] [WorldCat.org] [DOI] (P p)

S O Jensen, L S Thompson, E J Harry
Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly.
J Bacteriol: 2005, 187(18);6536-44
[PubMed:16159787] [WorldCat.org] [DOI] (P p)

Jennifer T Kemp, Adam Driks, Richard Losick
FtsA mutants of Bacillus subtilis impaired in sporulation.
J Bacteriol: 2002, 184(14);3856-63
[PubMed:12081956] [WorldCat.org] [DOI] (P p)

A Feucht, I Lucet, M D Yudkin, J Errington
Cytological and biochemical characterization of the FtsA cell division protein of Bacillus subtilis.
Mol Microbiol: 2001, 40(1);115-25
[PubMed:11298280] [WorldCat.org] [DOI] (P p)

Keisuke Fukuchi, Yasuhiro Kasahara, Kei Asai, Kazuo Kobayashi, Shigeki Moriya, Naotake Ogasawara
The essential two-component regulatory system encoded by yycF and yycG modulates expression of the ftsAZ operon in Bacillus subtilis.
Microbiology (Reading): 2000, 146 ( Pt 7);1573-1583
[PubMed:10878122] [WorldCat.org] [DOI] (P p)

X Wang, J Huang, A Mukherjee, C Cao, J Lutkenhaus
Analysis of the interaction of FtsZ with itself, GTP, and FtsA.
J Bacteriol: 1997, 179(17);5551-9
[PubMed:9287012] [WorldCat.org] [DOI] (P p)

M A Strauch
Delineation of AbrB-binding sites on the Bacillus subtilis spo0H, kinB, ftsAZ, and pbpE promoters and use of a derived homology to identify a previously unsuspected binding site in the bsuB1 methylase promote.
J Bacteriol: 1995, 177(23);6999-7002
[PubMed:7592498] [WorldCat.org] [DOI] (P p)

G Gonzy-Tréboul, C Karmazyn-Campelli, P Stragier
Developmental regulation of transcription of the Bacillus subtilis ftsAZ operon.
J Mol Biol: 1992, 224(4);967-79
[PubMed:1569582] [WorldCat.org] [DOI] (P p)